IMR Press / FBL / Volume 4 / Issue 4 / DOI: 10.2741/kennelly

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article
Life among the primitives: protein O-phosphatases in prokaryotes
Show Less
1 Department of Biochemistry, Virginia Tech, Blacksburg, VA 24061-0308, USA
Academic Editor:Norbert Berndt
Front. Biosci. (Landmark Ed) 1999, 4(4), 372–385; https://doi.org/10.2741/kennelly
Published: 15 March 1999
(This article belongs to the Special Issue Cellular functions of protein phosphatases)
Abstract

Prokaryotes contain at least five distinct families of protein O-phosphatases, including AceK, the chimeric isocitrate dehydrogenase kinase/phosphatase, and four protein phosphatase families first identified and characterized in Eukaryotes. The latter consist of the PPP and PPM families of protein-serine/threonine phosphatases, and the low molecular weight and conventional families of protein-tyrosine phosphatases. Prokaryotic protein O-phosphatases participate in the regulation of metabolic processes and the transduction of environmental signals. Certain pathogenic bacteria employ protein-tyrosine phosphatases as virulence factors, injecting them into host cells where they enzymatically perturb the phosphorylation state of proteins therein. While our understanding of protein O-phosphorylation events in Prokaryotes only now is emerging from its infancy, their phylogenetic diversity and malleability to genetic manipulation render these "simple'" organisms powerful vehicles for answering fundamental questions concerning the origins and evolution of this key biological regulatory mechanism.

Keywords
Protein Phosphorylation
Protein Phosphatases
Protein-Serine/Threonine Phosphatases
Protein-Tyrosine Phosphatases
Dual-Specific Protein Phosphatases
Bacteria
Archaea
Share
Back to top